BMRB Entry 25271

Name: NMR assignments of the prolyl peptidyl isomerase domain of the ribosome-associated molecular chaperone trigger factor from Escherichia coli
Published: 2019-07-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25271

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR assignments of the prolyl peptidyl isomerase domain of the ribosome-associated molecular chaperone trigger factor from Escherichia coli

Deposition date:

2014-10-07

Original release date:

2019-07-11

Authors:

Huang, Chih-Ting; Hsu, Shang-Te Danny

Citation:

Citation: Huang, Chih-Ting; Hsu, Shang-Te Danny. "NMR assignments of the peptidyl-prolyl cis-trans isomerase domain of trigger factor from E. coli." Biomol. NMR Assign. 10, 149-152 (2016).
PubMed: 26527152

Assembly members:

Assembly members:
trigger_factor, polymer, 99 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
trigger_factor: QATWKEKDGAVEAEDRVTID FTGSVDGEEFEGGKASDFVL AMGQGRMIPGFEDGIKGHKA GEEFTIDVTFPEEYHAENLK GKAAKFAINLKKVEERELP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	353
15N chemical shifts	96
1H chemical shifts	548

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPIase	1

Entities:

Entity 1, PPIase 99 residues - Formula weight is not available

1

GLN

ALA

THR

TRP

LYS

GLU

LYS

ASP

GLY

ALA

2

VAL

GLU

ALA

GLU

ASP

ARG

VAL

THR

ILE

ASP

3

PHE

THR

GLY

SER

VAL

ASP

GLY

GLU

PHE

4

GLU

GLY

LYS

ALA

SER

ASP

PHE

VAL

LEU

5

ALA

MET

GLY

GLN

GLY

ARG

MET

ILE

PRO

GLY

6

PHE

GLU

ASP

GLY

ILE

LYS

GLY

HIS

LYS

ALA

7

GLY

GLU

PHE

THR

ILE

ASP

VAL

THR

PHE

8

PRO

GLU

TYR

HIS

ALA

GLU

ASN

LEU

LYS

9

GLY

LYS

ALA

LYS

PHE

ALA

ILE

ASN

LEU

10

LYS

VAL

GLU

ARG

GLU

LEU

PRO

Samples:

PPIase: trigger factor, [U-98% 13C; U-98% 15N], 0.5 mM; D2O, [U-100% 2H], 10%; TRIS 20 mM; potassium chloride 100 mM; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	PPIase	isotropic	sample_conditions_1
2D 1H-13C HSQC	PPIase	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	PPIase	isotropic	sample_conditions_1
3D HNCO	PPIase	isotropic	sample_conditions_1
3D HNCACB	PPIase	isotropic	sample_conditions_1
3D CBCA(CO)NH	PPIase	isotropic	sample_conditions_1
3D C(CO)NH	PPIase	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks